The canonical helix of urea oligomers at atomic resolution: insights into folding-induced axial organization. - Université Pierre et Marie Curie Accéder directement au contenu
Article Dans Une Revue Angewandte Chemie International Edition Année : 2010

The canonical helix of urea oligomers at atomic resolution: insights into folding-induced axial organization.

Résumé

Graphical abstract : Helical by nature: Urea-based peptidomimetics with proteinogenic side chains are fully helical in the crystalline state (see picture). Four acyclic residues are sufficient to drive complete helix formation with all complementary H-bonding sites being satisfied (up to 14 for a 8-mer). Helices pack head-to-tail to create infinite H-bonded networks with different topologies.

Dates et versions

hal-00475693 , version 1 (22-04-2010)

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Citer

Lucile Fischer, Paul Claudon, Nagendar Pendem, Emeric Miclet, Claude Didierjean, et al.. The canonical helix of urea oligomers at atomic resolution: insights into folding-induced axial organization.. Angewandte Chemie International Edition, 2010, 49 (6), pp.1067-70. ⟨10.1002/anie.200905592⟩. ⟨hal-00475693⟩
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